Journal articles: 'Ideonella sakaiensis'

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Juliana, Sherina, Mia Parhusip, Argoby Simanullang, Elisabeth Tita, and Wahyu Irawati. "Potential of Ideonella sakaiensis bacteria in Degrading Plastic Waste Type Polyethylene Terephthalate." Jurnal Biologi Tropis 22, no. 2 (2022): 381–89. http://dx.doi.org/10.29303/jbt.v22i2.3321.

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Polyethylene terephathalate (PET) is a type of plastic content that is commonly is difficult to degrade so that it has an impact on global environmental problems. Plastic waste pollution needs to be overcome by using environmentally friendly methods to accelerate the PET plastic biodegradation process. Biodegradation is the use of microorganism activity to decompose plastic compounds so as to reduce the volume of waste. Ideonella sakaiensis is a bacterium that produces PETase enzymes that play a role in degrading PET. This literature review aims to determine the potential of Ideonella sakaiensis encoding the PETase gene in degrading polyethylene terephathalate plastic waste by discussing three focus studies, namely: 1) the potential of Ideonella sakaiensis, 2) the characteristics of polyethylene terephathalate plastic waste, 3) the relationship between the PETase coding gene and the degradation of polyethylene plastic waste terephathalate. Biodegradation of plastic waste Polyethylene terephathalate using Ideonella sakaiensis which has the potential to degrade PET faster with the PETase enzyme. The biodegradation mechanism carried out involves the process of transforming the PETase coding gene from I. sakaiensis to Escherichia coli bacteria influenced by pH and the effectiveness of the PETase enzyme work until the use of harvested products interacts with Polyethylene terephathalate plastic waste, which decomposes plastic waste.ÃÂ

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Pop, Cristian-Emilian, György Deák, Cristina Maria, et al. "Ideonella sakaiensis Can Metabolize Bisphenol A as a Carbon Source." Microorganisms 11, no. 12 (2023): 2891. http://dx.doi.org/10.3390/microorganisms11122891.

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Bisphenol A and its analogues represent a significant environmental and public health hazard, particularly affecting the endocrine systems of children and newborns. Due to the growing need for non-pathogenic biodegradation microbial agents as environmentally friendly and cost-effective solutions to eliminate endocrine disruptors, this study aimed to investigate the degradation of bisphenol A by Ideonella sakaiensis, based on its currently understood unique enzymatic machinery that is already well known for degrading polyethylene terephthalate. The present study provides novel insights into the metabolic competence and growth particularities of I. sakaiensis. The growth of I. sakaiensis exposed to bisphenol A exceeded that in the control conditions, starting with 72 h in a 70% nutrient-rich medium and starting with 48 h in a 100% nutrient-rich medium. Computational modeling showed that bisphenol A, as well as its analogue bisphenol S, are possible substrates of PETase and MHETase. The use of bisphenol A as a carbon and energy source through a pure I. sakaiensis culture expands the known substrate spectra and the species’ potential as a new candidate for bisphenol A bioremediation processes.

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Musdary, Fadhlan, Lisa Amalia, Reza Maulana Ahmad Lubis, and Widia Ningsih. "Systematic Review: Efektivitas Ideonella sakaiensis dan Chlamydomonas reinhardtii sebagai Agen Biodegradasi Plastik Berbahan Dasar PET." Jurnal Biolokus 4, no. 1 (2021): 20. http://dx.doi.org/10.30821/biolokus.v4i1.901.

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Bakteri Ideonella sakaiensis dan microalga Chlamydomonas reinhardtii dapat mendegradasi plastik PET (Poly-ethylene terephthalate) dengan mensintesiskan enzim PETase. Tujuan penelitian ini adalah untuk mengetahui efektivitas dari bakteri Ideonella sakaiensis dan Chlamydomonas reinhardtii sebagai agen biodegradasi plastik berbahan dasar PET. Penelitian ini merupakan systematic review, yang dilakukan dengan membandingkan dan menganalisis artikel-artikel yang diambil dari database digital seperti Springer Link dan Semanthic Schoolar. Artikel–artikel yang telah dicari dengan keyword yang telah ditentukan, kemudian dieksklusi sesuai dengan parameter yang ditetapkan, sehingga didapat 2 artikel rujukan. Hasil review menunjukkan bakteri I. sakaiensis mampu mendegradasi PET menjadi MHET (Monoterephtalic Hydroxyethyl Terephtalate) yang lebih dominan dibanding BHET (Bis-hydroxyethyl Terephtalate) &amp; TPA (Terephthalate Acid), sedangkan C. reinhardtii mendegradasikan PET menjadi TPA. Bakteri I. sakaiensis memerlukan waktu 18 jam untuk dapat mendegradasi 30 % dari PET film sedangkan C.reinhardtii memerlukan waktu 4 minggu untuk dapat mendegradasi 35,17% dari PET powder. Kedua mikroorganisme tersebut memiliki keefektifan yang berbeda dalam setiap parameter, yaitu hasil degradasi dan lama waktu pendegradasian.

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García, Mario D. "Depolymerization of polyethylene terephthalate by mutant variants of Ideonella sakaiensis PETase." Medwave 24, S2 (2024): eUTA12. https://doi.org/10.5867/medwave.2024.s2.uta12.

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Introducción La depolimerización enzimática de PET es una tecnología prometedora para el reciclaje de residuos de PET. Es un proceso ecológico y sostenible que utiliza enzimas para descomponer el PET en sus monómeros, ácido tereftálico (TPA) y etilenglicol (EG). En los últimos años se han producido importantes avances en la depolimerización enzimática del PET. Uno de los avances más importantes es el descubrimiento de nuevas enzimas que degradan el PET, incluyendo la enaima PETasa de Ideonella sakaiensis. Estas enzimas son más eficientes y selectivas que las enzimas cutinasas de Fusarium solani o Thermobifida fusca, que fueron los primeros referentes para el tratamiento enzimático del PET, y pueden despolimerizar el PET a temperaturas y presiones más bajas. Otro avance importante es el desarrollo de nuevos métodos para mejorar la eficiencia de la despolimerización enzimática del PET. Estos métodos incluyen el tratamiento previo de los residuos de PET para hacerlos más accesibles a las enzimas y el uso de enzimas inmovilizadas para mejorar la estabilidad y la reutilización de las enzimas. Como resultado de estos avances, la despolimerización enzimática del PET se está convirtiendo en una opción más viable para el reciclaje de residuos de PET. Se trata de una tecnología prometedora que podría ayudar a reducir la cantidad de residuos de PET que acaban en los vertederos y en el medio ambiente. Objetivos El objetivo del presente estudio fue identificar variantes mutantes de la enzima PETasa de Ideonella sakaiensis con mayor termoestabilidad y actividad degradadora de PET Método Las variantes mutantes de la enzima PETasa de Ideonella sakaiensis fueron obtenidas mediante diseño racional de su sitio activo. Primeramente, se identificó residuos clave para la unión del sustrato a la enzima y se determinó posibles substituciones mediante análisis de homología de secuencia con enzimas cutinasas. Las posibles mutaciones se evaluaron mediante dinámica molecular y las substituciones que presentaron mejor afinidad hacia el PET, de acuerdo a la energía de Gibbs calculada para la unión del sustrato al sitio activo, fueron construidas mediante varias iteraciones de PCR mutagénica. Las enzimas fueron sobreexpresadas en Escherichia coli BL21 mediante el uso de vectores de expresión y fueron purificadas mediante cromatografía de afinidad. La actividad y termoestabilidad de las enzimas fueron evaluadas empleando films de PET obtenidos de botellas plásticas comerciales. Principales resultados Se desarrollaron seis nuevas variantes mutantes de la enzima PETasa de Ideonella sakaiensis que presentan mayor termoestabilidad y capacidad para degradar el PET. La termoestabilidad de las variantes mutantes se incrementó en aproximadamente 10 a 15 °C, mientras que la actividad de la enzima se incrementó en aproximadamente 3 veces con respecto a la enzima silvestre. Conclusiones La despolimerización enzimática de PET es una alternativa amigable con el medio ambiente y en rápido desarrollo con el potencial de tener un impacto significativo en el reciclaje de residuos de PET. Las variantes mutantes de la enzima PETasa de ideonella sakaiensis muestran mayor termoestabilidad y actividad que la enzima silvestre y constituyen herramientas importantes para el desarrollo de sistemas de reciclaje enzimático del PET a gran escala.

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Jaydev, Misra, and Mallick Priyadarshini. "Managing wastewater using plastic eating bacteria – A sustainable solution for sewage fed fisheries." Journal of Indian Chemical Society Vol. 97, Apr 2020 (2020): 513–19. https://doi.org/10.5281/zenodo.5638301.

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Department of Economics, Dhruba Chand Halder College, Dakshin Barasat-743 372, South 24-Parganas, West Bengal, India Department of Microbiology, Asutosh College, Kolkata-700 026, India E-mail: priyadm1@yahoo.com Manuscript received online 14 December 2019, accepted 06 March 2020 Affluent like plastics has made the water management issues of sewage fed fisheries much more difficult as well as costineffective. However, possible impact of introduction of bacteria in managing plastics in wastewater for sustainable sewage fed fisheries operation has not been yet documented. Present study is an attempt to investigate whether Ideonella sakaiensis can be used to eradicate problems with plastics in sewage water so that fisheries operation can be continued in a sustainable way. The objective is to find the best suitable degradation procedure of various kinds of plastic involving biological means as well as other sources of natural means too. Bacterial and fungal species were also widely employed in these degradation processes. Several strains of Ideonella sakaiensis were used in developing the desired process. It was observed that, the hydrocarbon, present in plastics, can be degraded by organisms which can also use it as proper sources of carbon and these organisms can be employed. The outcomes are established by the changes in weight differences, tensile strength and reduction in the viscous properties in most of the instances while in few cases, molecular weight distribution, and fragility was also noticed. Thus it can be also concluded that HDPE plastics shows more resistance to soil conditions than that of the LDPE plastics. Further, Ideonella sakaiensis as a species does not pose any threat to the growth and cultivation of fishes. Thus in near future, plastics causing pollution in wastewater can be treated using this special variety of bacteria for improvement of fish cultivation.

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BOROS, KRISZTINA, ILKA HORVATH, CATALINA ROTARU, RALUCA BIANCA TOMOIAGA, MONICA IOANA TOȘA, and LASZLO-CSABA BENCZE. "PETase from Ideonella sakaiensis: towards facile bacterial expression system." Romanian Biotechnological Letters 27, no. 2/2022 (2022): 3507–16. http://dx.doi.org/10.25083/rbl/27.3/3507.3516.

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One of the most promising PET-hydrolysing enzyme, IsPETase, originates from 'plastic-consuming' bacteria Ideonella sakaiensis and operates at moderate temperatures (30-40 °C) in aqueous environment, showing far higher hydrolysing efficiency than several cutinases. Accordingly, the development of proper recombinant expression system providing facile access to the isolated/purified IsPETase is also of high interest. In our aim to produce active recombinant IsPETase, the unsuccessful expression registered by employing several reported expression systems, directed us towards the optimization/ development of a facile/accessible recombinant expression system suitable for IsPETase production. Testing several plasmid constructs, providing different N- or C-terminal affinity tags for the expression of full-length or truncated (residues 28-290) IsPETase and various E. coli expression hosts, revealed several non-reported issues hindering the recombinant expression of IsPETase. After optimization of the construct and expression host, the use of N-terminal His-tag and Rosetta-gami B expression host provided recombinant IsPETase in high purity and titer-yield. The thermal denaturation profile and PET-hydrolysing activity of the obtained IsPETase agree with the reported data, supporting proper folding of the purified protein. The results support that the in vivo folding process of IsPETase might be differently affected among the different E. coli host strains, moreover, underline the importance of the proper selection of the cloning strategy for the successful expression of the IsPETase.

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Sevilla, Maria Eduarda, Mario D. Garcia, Yunierkis Perez-Castillo, et al. "Degradation of PET Bottles by an Engineered Ideonella sakaiensis PETase." Polymers 15, no. 7 (2023): 1779. http://dx.doi.org/10.3390/polym15071779.

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Extensive plastic production has become a serious environmental and health problem due to the lack of efficient treatment of plastic waste. Polyethylene terephthalate (PET) is one of the most used polymers and is accumulating in landfills or elsewhere in nature at alarming rates. In recent years, enzymatic degradation of PET by Ideonella sakaiensis PETase (IsPETase), a cutinase-like enzyme, has emerged as a promising strategy to completely depolymerize this polymer into its building blocks. Here, inspired by the architecture of cutinases and lipases homologous to IsPETase and using 3D structure information of the enzyme, we rationally designed three mutations in IsPETase active site for enhancing its PET-degrading activity. In particular, the S238Y mutant, located nearby the catalytic triad, showed a degradation activity increased by 3.3-fold in comparison to the wild-type enzyme. Importantly, this structural modification favoured the function of the enzyme in breaking down highly crystallized (~31%) PET, which is found in commercial soft drink bottles. In addition, microscopical analysis of enzyme-treated PET samples showed that IsPETase acts better when the smooth surface of highly crystalline PET is altered by mechanical stress. These results represent important progress in the accomplishment of a sustainable and complete degradation of PET pollution.

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Muhammad Latif NAZIROV, Ilxom XALILOV,, and Fazliddin QOBILOV,. "POLIETILENNI SAMARALI PARCHALASH UCHUN PETaza FERMENTINI ESCHERICHIA COLI BAKTERIYASIDA EXSPRESSIYALASH." UzMU xabarlari 3, no. 3.1 (2024): 81–85. http://dx.doi.org/10.69617/uzmu.v3i3.1.1718.

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Plastik ifloslanish, birinchi navbatda, polietilen tereftalat (PET) plastmassalari bilan bog'liq bo'lib, jiddiy global ekologik inqirozga aylandi. Bakteriyaning Ideonella sakaiensis 201-F6 turi shtami PETni parchalash uchun eng samaralii yechim sifatida foydalaniladi. Biz ushbu maqolada, termostabil mutatsiyalarga ega bo’lgan FAST-PETaza fermentini klonlash va uni E.coli bakteriyasida ekspressiyalash, oqsilni nikel xelat xromotagrafiya usulida tozalab olish va ferment aktivligini aniqlash kabi tadqiqot natijalarini bayon etdik. Tadqiqot natijalari aktivlikga ega bo’lgan FAST-PETaza fermentini samarali tozalab olinganini ko’rsatdi.

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Muhammad Latif NAZIROV, Ilxom XALILOV,, and Fazliddin QOBILOV,. "POLIETILENNI SAMARALI PARCHALASH UCHUN PETaza FERMENTINI ESCHERICHIA COLI BAKTERIYASIDA EXSPRESSIYALASH." UzMU xabarlari 3, no. 3.1 (2024): 81–85. https://doi.org/10.69617/nuuz.v3i3.1.1718.

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Plastik ifloslanish, birinchi navbatda, polietilen tereftalat (PET) plastmassalari bilan bog'liq bo'lib, jiddiy global ekologik inqirozga aylandi. Bakteriyaning Ideonella sakaiensis 201-F6 turi shtami PETni parchalash uchun eng samaralii yechim sifatida foydalaniladi. Biz ushbu maqolada, termostabil mutatsiyalarga ega bo’lgan FAST-PETaza fermentini klonlash va uni E.coli bakteriyasida ekspressiyalash, oqsilni nikel xelat xromotagrafiya usulida tozalab olish va ferment aktivligini aniqlash kabi tadqiqot natijalarini bayon etdik. Tadqiqot natijalari aktivlikga ega bo’lgan FAST-PETaza fermentini samarali tozalab olinganini ko’rsatdi.

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Cerda-Mejía, Liliana, and Mario D. García. "Rational design of Ideonella sakaiensis PET hydrolase for suistanable PET recycling." Medwave 24, S2 (2024): eUTA11. https://doi.org/10.5867/medwave.2024.s2.uta11.

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Introducción La enzima PETasa de Ideonella sakaiensis (IsPETasa) es una hidrolasa similar a las cutinasas que, en coordinación con la enzima MHET hidrolasa permite a I. sakaiensis alimentan de plásticos PET como única fuente de carbono y energía. IsPETasa es capaz de descomponer el plástico PET en sus componentes básicos (MHET, TPA o BHET), lo que la convierte en una herramienta potencialmente útil para el reciclaje biológico del PET que se acumula en vertederos o en cualquier otro lugar del medio ambiente. Además, la utilización de IsPETasa puede contribuir a reducir la cantidad de plástico que se produce anulmente a partir de combustibles fósiles, ya que los productos de la descompocición del PET podrían ser utilizados para producir nuevo plástico con características idénticas a las del plástico virgen, y de esta manera, reutilizar los residuos de PET de manera más eficiente. Objetivos El objetivo del presente estudio fue desarrollar una enzima PETasa con una mayor capacidad de degradar el PET empleando métodos de diseño racional de su sitio activo. Método Se realizó dinámicas moleculares cortas para simular la unión del sustrato a la enzima, tanto para la variante silvestre como para las variantes mutantes diseñadas. Las mutaciones que arrojaron los mejores resultados fueron introducidas en la enzima mediante PCR. Las enzimas fueron expresadas en E. coli y purificadas mediante cromatografía. Las enzimas purificadas se incubaron con films de PET por varios días y caracterizadas mediante SEM, AFM y DSC. Principales resultados Se obtuvieron tres variantes mutantes (I208V, N212A y S238Y) que presentaron capacidades diferentes para degradar el PET en comparación a la variante silvestre. Conclusiones El diseño racional de enzimas permitió desarrollar variantes mutantes de la enzima IsPETasa que mostraron mayor actividad degradadora del PET

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Liu, Congcong, Chao Shi, Sujie Zhu, Risheng Wei, and Chang-Cheng Yin. "Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis." Biochemical and Biophysical Research Communications 508, no. 1 (2019): 289–94. http://dx.doi.org/10.1016/j.bbrc.2018.11.148.

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Son, Hyeoncheol Francis, Seongjoon Joo, Hogyun Seo, et al. "Structural bioinformatics-based protein engineering of thermo-stable PETase from Ideonella sakaiensis." Enzyme and Microbial Technology 141 (November 2020): 109656. http://dx.doi.org/10.1016/j.enzmictec.2020.109656.

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Bradshaw, Aaron. "Can Microbes Be Active Participants in Research? Developing a Methodology for Collaborating with Plastic-Eating Microbes." Environmental Humanities 14, no. 2 (2022): 284–302. http://dx.doi.org/10.1215/22011919-9712379.

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Abstract The emergence of Ideonella sakaiensis, a microorganism with the capacity to metabolize the widely used plastic polyethylene terephthalate (PET), raises important questions about how human and nonhuman agency are related in responding to pressing environmental issues. The article explores how the agency and expertise of I. sakaiensis is a constitutive but often overlooked collaborator in scientific research into plastic biodegradation, and it attempts to develop a methodology for enrolling microorganisms as active research participants from the outset. Knowledge coproduced with microbial others, and specifically those microbes with the capacity to detoxify anthropogenic pollutants, may inform and enact inclusive and prescient responses to ongoing environmental degradation. Accordingly, drawing from theoretical orientations in more-than-human participatory research and animals’ geographies, the article asks how microorganisms might express their own directives, preferences, and constraints on the research process, and how, in turn, we might listen and be directed by them. Although the ontological and ethical commitments of the environmental humanities are well suited for welcoming microbes as partners in deliberative processes, the challenges of communicating with them across vast scalar and bodily differences suggests a need to engage with techniques traditionally considered the disciplinary property of the natural sciences. Some of these concepts are contextualized with respect to a research project currently being undertaken at the River Lea in East London and the attempt to enroll I. sakaiensis as a collaborator in responding to plastic pollution in the river.

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Tanasupawat, Somboon, Toshihiko Takehana, Shosuke Yoshida, Kazumi Hiraga, and Kohei Oda. "Ideonella sakaiensis sp. nov., isolated from a microbial consortium that degrades poly(ethylene terephthalate)." International Journal of Systematic and Evolutionary Microbiology 66, no. 8 (2016): 2813–18. http://dx.doi.org/10.1099/ijsem.0.001058.

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Zara, Zeenat, Deepti Mishra, Saurabh Kumar Pandey, et al. "Surface Interaction of Ionic Liquids: Stabilization of Polyethylene Terephthalate-Degrading Enzymes in Solution." Molecules 27, no. 1 (2021): 119. http://dx.doi.org/10.3390/molecules27010119.

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The effect of aqueous solutions of selected ionic liquids solutions on Ideonella sakaiensis PETase with bis(2-hydroxyethyl) terephthalate (BHET) substrate were studied by means of molecular dynamics simulations in order to identify the possible effect of ionic liquids on the structure and dynamics of enzymatic Polyethylene terephthalate (PET) hydrolysis. The use of specific ionic liquids can potentially enhance the enzymatic hydrolyses of PET where these ionic liquids are known to partially dissolve PET. The aqueous solution of cholinium phosphate were found to have the smallest effect of the structure of PETase, and its interaction with (BHET) as substrate was comparable to that with the pure water. Thus, the cholinium phosphate was identified as possible candidate as ionic liquid co-solvent to study the enzymatic hydrolyses of PET.

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Barbosa, Gecielly de Souza, Paloma Alves Soares, Victória Roberta Neves dos Santos, et al. "Ideonella sakaiensis and action de its depolymerizing enzymes of Polyethylene terephthalate (PET): a literature review." IJS - International Journal of Sciences 3, no. 2 (2022): 9–12. http://dx.doi.org/10.29327/229003.3.2-3.

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Seo, Hogyun, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, and Kyung-Jin Kim. "Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli." Biochemical and Biophysical Research Communications 508, no. 1 (2019): 250–55. http://dx.doi.org/10.1016/j.bbrc.2018.11.087.

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Son, Hyeoncheol Francis, In Jin Cho, Seongjoon Joo, et al. "Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation." ACS Catalysis 9, no. 4 (2019): 3519–26. http://dx.doi.org/10.1021/acscatal.9b00568.

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Uday, J. "Molecular docking analysis of PET with MHET." Bioinformation 19, no. 3 (2023): 255–59. http://dx.doi.org/10.6026/97320630019255.

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An estimated 311 million tons of plastics are produced annually worldwide; 90% of these are derived from petrol. A considerable portion of these plastics is used for packaging (such as drinking bottles), but only ~14% is collected for recycling. Most plastics degrade extremely slowly, thus constituting a major environmental hazard, especially in the oceans, where microplastics are a matter of major concern. One potential solution for this problem is the synthesis of degradable plastics from renewable resources. From the microbial consortium, the researchers isolated a unique bacterium Ideonella sakaiensis 201-F6 that could almost completely degrade a thin film of PET in a short span of six weeks at 30°C. The objective of the present study is to identify the ligands that may be exploited to improve catalysis and expand substrate specificity and thus significantly advance enzymatic plastic polymer degradation.

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Lee, Seul Hoo, Dongwoo Ki, and Kyung-Jin Kim. "Purification, crystallization, and X-ray crystallographic analysis terephthalic acid binding protein from Ideonella sakaiensis." Korean Society for Structural Biology 11, no. 1 (2023): 16–19. http://dx.doi.org/10.34184/kssb.2023.11.1.16.

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Sanjogdeep, Kaur Zorawar Singh and Baani Singh. "Plastic-eating Bacteria as a Remedy for Plastic Pollution." Environmental Science Archives 4, no. 1 (2025): 14–20. https://doi.org/10.5281/zenodo.14584887.

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Plastic pollution can have negative effects on human health as well as serious effects on marine ecosystems. The widespread production of polyethylene terephthalate (PET) single-use plastics poses a significant threat to aquatic and terrestrial ecosystems in terms of plastic waste. PET is a strong, clear and light plastic that is typically used for food and beverage packaging, as well as for other single-use applications. As a result, removing plastic from the environment is not only difficult but also ineffective financially. Numerous strains of bacteria are capable of biodegrading a variety of plastics. Utilizing beneficial micro-organisms that are capable of breaking down plastic could be an effective and long-term solution to all of the problems. Ideonella sakaeinsis 201-F6 is the most well-known heterotrophic bacteria that can use PET as its primary source of energy and carbon to degrade plastic in the environment. It has a place with the sort of Ideonella and the family Comamonadaceae. With the assistance of specific enzymes like PETase and MHETase, it can ultimately degrade plastic, potentially reducing the problem of plastic waste. Polyethylene terephthalate (PET) is first transformed by the PETase into mono-(2-hydroxyethyl) terephthalate (MHET), after which MHET is hydrolyzed to produce ethylene glycol (EG) and terephthalic acid (TPA). I.  sakaiensis offers a novel strategy for recycling PET because it can mediate the direct transformation of non-biodegradable PET into plastic that is better for the environment.

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Wagner-Egea, Paula, Virginia Tosi, Ping Wang, Carl Grey, Baozhong Zhang, and Javier A. Linares-Pastén. "Assessment of IsPETase-Assisted Depolymerization of Terephthalate Aromatic Polyesters and the Effect of the Thioredoxin Fusion Domain." Applied Sciences 11, no. 18 (2021): 8315. http://dx.doi.org/10.3390/app11188315.

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Terephthalate polyesters such as poly(ethylene terephthalate) (PET) have been massively produced over the last few decades due to their attractive properties in multiple applications. However, due to their limited biodegradability, they have accumulated in landfills and oceans, posing an environmental threat. Enzymatic recycling technologies are predicted to generate long-term socioeconomic benefits. In the present work, we compared the IsPETase (from Ideonella sakaiensis 201-F6) activity on a series of polyesters, including poly(butylene) terephthalate (PBT), poly(hexamethylene) terephthalate (PHT) and Akestra™, with PET. The IsPETase showed remarkable activity toward PET (39% degradation of the original polyester) that was higher than that toward Akestra™ (0.13%), PBT (0.25%) and PHT (0.13%) after 72 h. Thus, based on experimental data and computational analysis, we report insights into IsPETase activity on a series of terephthalate-based polyesters. Aside from that, the fusion domain (Trx) effect in the production and activity of a recombinant Trx-IsPETase is reported.

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Menzel, Teresa, Sebastian Weigert, Andreas Gagsteiger, et al. "Impact of Enzymatic Degradation on the Material Properties of Poly(Ethylene Terephthalate)." Polymers 13, no. 22 (2021): 3885. http://dx.doi.org/10.3390/polym13223885.

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With macroscopic litter and its degradation into secondary microplastic as a major source of environmental pollution, one key challenge is understanding the pathways from macro- to microplastic by abiotic and biotic environmental impact. So far, little is known about the impact of biota on material properties. This study focuses on recycled, bottle-grade poly(ethylene terephthalate) (r-PET) and the degrading enzyme PETase from Ideonella sakaiensis. Compact tension (CT) specimens were incubated in an enzymatic solution and thermally and mechanically characterized. A time-dependent study up to 96 h revealed the formation of steadily growing colloidal structures. After 96 h incubation, high amounts of BHET dimer were found in a near-surface layer, affecting crack propagation and leading to faster material failure. The results of this pilot study show that enzymatic activity accelerates embrittlement and favors fragmentation. We conclude that PET-degrading enzymes must be viewed as a potentially relevant acceleration factor in macroplastic degradation.

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Liu, Bing, Lihui He, Liping Wang, et al. "Protein Crystallography and Site‐Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis." ChemBioChem 19, no. 14 (2018): 1471–75. http://dx.doi.org/10.1002/cbic.201800097.

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Sagong, Hye-Young, Hyeoncheol Francis Son, Hogyun Seo, Hwaseok Hong, Donghoon Lee, and Kyung-Jin Kim. "Implications for the PET decomposition mechanism through similarity and dissimilarity between PETases from Rhizobacter gummiphilus and Ideonella sakaiensis." Journal of Hazardous Materials 416 (August 2021): 126075. http://dx.doi.org/10.1016/j.jhazmat.2021.126075.

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Ho, Ngai Hei Ernest, Sefli Sri Wahyu Effendi, Wan-Wen Ting, et al. "Heterologous expression and characterization of Aquabacterium parvum lipase, a close relative of Ideonella sakaiensis PETase in Escherichia coli." Biochemical Engineering Journal 197 (August 2023): 108985. http://dx.doi.org/10.1016/j.bej.2023.108985.

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Lin, Lee Yi, Nardiah Rizwana Jaafar, Jonathan Guyang Ling, et al. "Cross-linked enzyme aggregates of polyethylene terephthalate hydrolyse (PETase) from Ideonella sakaiensis for the improvement of plastic degradation." International Journal of Biological Macromolecules 263 (April 2024): 130284. http://dx.doi.org/10.1016/j.ijbiomac.2024.130284.

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Rennison, Andrew, Jakob R. Winther, and Cristiano Varrone. "Rational Protein Engineering to Increase the Activity and Stability of IsPETase Using the PROSS Algorithm." Polymers 13, no. 22 (2021): 3884. http://dx.doi.org/10.3390/polym13223884.

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Polyethylene terephthalate (PET) is the most widely used polyester plastic, with applications in the textile and packaging industry. Currently, re-moulding is the main path for PET recycling, but this eventually leads to an unsustainable loss of quality; thus, other means of recycling are required. Enzymatic hydrolysis offers the possibility of monomer formation under mild conditions and opens up alternative and infinite recycling paths. Here, IsPETase, derived from the bacterium Ideonella sakaiensis, is considered to be the most active enzyme for PET degradation under mild conditions, and although several studies have demonstrated improvements to both the stability and activity of this enzyme, stability at even moderate temperatures is still an issue. In the present study, we have used sequence and structure-based bioinformatic tools to identify mutations to increase the thermal stability of the enzyme so as to increase PET degradation activity during extended hydrolysis reactions. We found that amino acid substitution S136E showed significant increases to activity and stability. S136E is a previously unreported variant that led to a 3.3-fold increase in activity relative to wild type.

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Wagner-Egea, Paula, Lucía Aristizábal-Lanza, Cecilia Tullberg, et al. "Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization." Catalysts 13, no. 9 (2023): 1234. http://dx.doi.org/10.3390/catal13091234.

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Enzymatic polyethylene terephthalate (PET) recycling processes are gaining interest for their low environmental impact, use of mild conditions, and specificity. Furthermore, PET hydrolase enzymes are continuously being discovered and engineered. In this work, we studied a PET hydrolase (PET2), initially characterized as an alkaline thermostable lipase. PET2 was produced in a fusion form with a 6-histidine tag in the N-terminal. The PET2 activity on aromatic terephthalate and new indole-based polyesters was evaluated using polymers in powder form. Compared with IsPETase, an enzyme derived from Ideonella sakaiensis, PET2 showed a lower PET depolymerization yield. However, interestingly, PET2 produced significantly higher polybutylene terephthalate (PBT) and polyhexylene terephthalate (PHT) depolymerization yields. A clear preference was found for aromatic indole-derived polyesters over non-aromatic ones. No activity was detected on Akestra™, an amorphous copolyester with spiroacetal structures. Docking studies suggest that a narrower and more hydrophobic active site reduces its activity on PET but favors its interaction with PBT and PHT. Understanding the enzyme preferences of polymers will contribute to their effective use to depolymerize different types of polyesters.

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Yang, Jun, Binyang Deng, Pingan Liao, et al. "Improving the Catalytic Activity and Thermostability of FAST-PETase with a Multifunctional Short Peptide." Biomolecules 15, no. 6 (2025): 888. https://doi.org/10.3390/biom15060888.

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Previous reports indicated that self-assembling amphipathic peptide S1v1 (AEAEAHAH)2 significantly enhances the soluble expression, thermostability, and activity of the target proteins when fused to them. In order to obtain high-efficiency enzymes for the large-scale degradation of polyethylene terephthalate (PET), this multifunctional peptide was fused to the N- and C-terminus of FAST-PETase, a variant of Ideonella sakaiensis PETase (IsPETase), with a PT-linker (TTVTTPQTS) harbored between the target protein and the multifunctional peptide. Consistent with previous reports, S1v1 increased the solubility of FAST-PETase slightly. Moreover, it increased the activity of FAST-PETase dramatically. The amount of terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthalic acid (MHET) released from PET substrate after 24 h of digestion at 50°C by fusion enzymes bearing N- and C-terminal S1v1 tag was approximately 2.9- and 4.6-fold that of FAST-PETase, respectively. Furthermore, the optimal temperature and thermostability of the fusion proteins increased in comparison with FAST-PETase. The present study provides a novel strategy to improve the depolymerization efficiency of FAST-PETase.

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Igiebor, F. A., E. M. Jonathan, O. Haruna, and B. I. Alenkhe. "Plastics Biodegradation: The Situation Now and Its Potential Effects on Environmental Safety." Journal of Applied Sciences and Environmental Management 28, no. 1 (2024): 165–78. http://dx.doi.org/10.4314/jasem.v28i1.19.

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Plastics are made of polymers with a high concentration of petrochemical components derived from coal, oil, and natural gas and majority of fossil and bio-based plastics are not biodegradable. The aim of this paper is to provide a critical review of the current situation and potential environmental safety of plastic biodegradation by harvesting data and information from secondary sources. Data obtained show that there are several different kinds of plastics exists, including polypropylene (PE), polyethylene terephthalate (PET), polyvinyl chloride (PVC), high-density polyethylene (HDPE), low-density polyethylene (LDPE), and polystyrene (PS) and that the environment is seriously threatened by the widespread use of plastics, poor waste management, and careless community behaviour about proper disposal. In Nigeria, more than 88% of the plastic garbage produced is not recycled. In the absence of appropriate waste management and litter control techniques, the use of biodegradable plastics for specialised applications is a promising idea. Ideonella sakaiensis 201-F6 is a brand-new bacterial strain that has been discovered to be capable of breaking down PET. High-density polyethylene was found to be negatively impacted by Achromobacter xylosoxidans. Therefore, a lot of research is being done to create methods for degrading polymers composed of fossil and biological sources as excellent techniques and environmentally acceptable strategies for waste management.

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Abidin, Nurul, Wahdaniar, Novi Febrianti, and Sharfina Mutia Syarifah. "Pengurai Sampah Plastik Ramah Lingkungan." Bincang Sains dan Teknologi 2, no. 02 (2023): 63–71. http://dx.doi.org/10.56741/bst.v2i02.339.

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Tujuan dari penelitian ini adalah untuk menyelidiki mekanisme penguraian sampah plastik oleh berbagai mikroorganisme, termasuk bakteri, cendawan, dan ulat. Hasil penelitian menunjukkan bahwa mekanisme penguraian plastik melibatkan berbagai strategi biokimia dan enzimatik yang berbeda pada setiap mikroorganisme. Bakteri seperti Ideonella sakaiensis 201-F6 memiliki enzim PETase yang mampu mengurai plastik PET menjadi senyawa monomer yang lebih sederhana. Cendawan seperti Trichoderma viride dan Aspergillus nomius juga memiliki enzim ekstraseluler dan kemampuan untuk mengurai berbagai jenis plastik. Sementara itu, ulat Galleria mellonella dan larva Tenebrio molitor menggunakan mekanisme pencernaan yang melibatkan enzim dan kerjasama dengan bakteri dalam sistem pencernaan mereka. Ulat G. mellonella memakan plastik polyethylene (PE) yang mirip dengan struktur karbon lilin lebah yang menjadi sumber makanan alaminya, sementara larva T. molitor memakan plastik polystyrene (PS) dan menghasilkan enzim serta bakteri dalam sistem pencernaannya untuk menguraikan styrofoam menjadi senyawa organik yang lebih sederhana. Mekanisme penguraian sampah plastik oleh mikroorganisme masih dalam tahap penelitian yang terus berkembang, dan masih banyak hal yang perlu dipahami dengan lebih mendalam. Penelitian lebih lanjut diperlukan untuk mengidentifikasi enzim, jalur metabolic, dan mekanisme detil lainnya yang terlibat dalam penguraian sampah plastik oleh mikroorganisme. Penemuan lebih lanjut tentang mekanisme ini dapat berpotensi menjadi sumber inspirasi untuk pengembangan teknologi bioteknologi yang dapat membantu mengurangi masalah sampah plastik.

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Kaur, Kohinoor, Samiksha Sharma, Nidhi Shree, and Rekha Mehrotra. "Recent Advancements and Mechanism of Plastics Biodegradation Promoted by Bacteria: A Key for Sustainable Remediation for Plastic Wastes." Biosciences Biotechnology Research Asia 20, no. 1 (2023): 1–12. http://dx.doi.org/10.13005/bbra/3063.

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ABSTRACT: Plastic has become an indispensable part of our lives and cutting down plastic consumption entirely is difficult to achieve. The recalcitrant and non-biodegradable nature of plastic leads to accumulation of tons of plastic in landfills and water bodies which further risks marine life and human life too causing serious health issues. In recent years, several microbial enzymes have been discovered that have the ability to degrade plastic. The present review highlights the recent discovery and properties of the plastic-eating bacteria, Ideonella sakaiensis, that has potential to be used for plastic degradation and recycling. The bacteria possess unique enzymes that allow it to utilise Polyethylene terephthalate (PET) plastic, thereby degrading it to relatively safer monomeric forms that can be further degraded and purified to manufacture recycled plastics. The review focuses on the mechanism of PET hydrolysis, recent advances in the field to escalate enzymatic efficiency and development of new bacterial and enzymatic strains through genetic engineering which can enhance its catalytic competence and make the process time and cost-effective. The plastic metabolising bacteria can thus be a potential and efficient bio-alternative to degrade plastic in a biological and sustainable manner thereby helping scale the otherwise insurmountable plastic pollution crisis.

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Janatunaim, Rifqi Z., and Azzania Fibriani. "Construction and Cloning of Plastic-degrading Recombinant Enzymes (MHETase)." Recent Patents on Biotechnology 14, no. 3 (2020): 229–34. http://dx.doi.org/10.2174/1872208314666200311104541.

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Background: Polyethylene terephthalate (PET) is the most widely produced polyester plastic in the world. PET is very difficult to catalyze or biological depolymerization due to the limited access to ester bonds. Consequently, plastic will be stockpiled or flowed into the environment which is projected until hundreds of years. The most effective and environmental friendly plastic degradation method is biodegradation with microorganisms. Two specific enzyme for PET hydrolase, PETase and MHETase have been identified from Ideonella sakaiensis 201-F6. Recombinant genes are made to increase the effectiveness of enzymes in degrading PET. Previous studies of the PETase gene have been carried out, but to produce the final degradation PET product, the enzyme MHETase is needed. Thus, in this study the MHETase gene construction was carried out. Methods: The goal of this study is to construct MHETase gene in pUCIDT plasmid with native signal peptide from I. sakaensis 201-F6 and constitutive promoter J23106 was expressed in Escherichia coli BL21 (DE3) by heats shock. Expression analysis using SDS-PAGE and activity of enzyme is analyzed by spectrophotometry method and SEM. Results: MHETase gene protein was successfully constructed in pUCIDT +Amp plasmid with native signal peptide from Ideonella sakaensis 201-F6, T7 terminator and constitutive promoter J23106. PCR analysis showed that the gene successfully contained in the cells by band size (1813 bp) in electrophoresis gel. Analysis using Snap Gene, pairwise alignment using MEGA X, and NCBI was demonstrated that MHETase sequence the gene was in-frame in pUCIDT plasmid. Conclusion: MHETase gene was successfully constructed in plasmids by in silico method. Synthetic plasmids transformed in E. coli BL21 (DE3) contain MHETase gene sequences which were in frame. Hence, the E. coli BL21 (DE3) cells have the potential to produce MHETase proteins for the plastic degradation testing process. We will patent the construct of MHETase gene using constitutive promoter and signal peptide from native which expressed in E. coli BL21 (DE3). This patent refers to a more applicable plastic degradation system with a whole cell without the need for purification and environmental conditioning of pure enzymes.

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Wallace, Noah E., Mary C. Adams, Andrew C. Chafin, Diamonte D. Jones, Caroline L. Tsui, and Todd D. Gruber. "The highly crystalline PET found in plastic water bottles does not support the growth of the PETase ‐producing bacterium Ideonella sakaiensis." Environmental Microbiology Reports 12, no. 5 (2020): 578–82. http://dx.doi.org/10.1111/1758-2229.12878.

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Liu, Bing, Lihui He, Liping Wang, et al. "Cover Feature: Protein Crystallography and Site‐Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis (ChemBioChem 14/2018)." ChemBioChem 19, no. 14 (2018): 1464. http://dx.doi.org/10.1002/cbic.201800330.

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Pirillo, Valentina, Marco Orlando, Davide Tessaro, Loredano Pollegioni, and Gianluca Molla. "An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes." International Journal of Molecular Sciences 23, no. 1 (2021): 264. http://dx.doi.org/10.3390/ijms23010264.

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Enzymatic degradation is a promising green approach to bioremediation and recycling of the polymer poly(ethylene terephthalate) (PET). In the past few years, several PET-hydrolysing enzymes (PHEs) have been discovered, and new variants have been evolved by protein engineering. Here, we report on a straightforward workflow employing semi-rational protein engineering combined to a high-throughput screening of variant libraries for their activity on PET nanoparticles. Using this approach, starting from the double variant W159H/S238F of Ideonella sakaiensis 201-F6 PETase, the W159H/F238A-ΔIsPET variant, possessing a higher hydrolytic activity on PET, was identified. This variant was stabilized by introducing two additional known substitutions (S121E and D186H) generating the TS-ΔIsPET variant. By using 0.1 mg mL−1 of TS-ΔIsPET, ~10.6 mM of degradation products were produced in 2 days from 9 mg mL−1 PET microparticles (~26% depolymerization yield). Indeed, TS-ΔIsPET allowed a massive degradation of PET nanoparticles (>80% depolymerization yield) in 1.5 h using only 20 μg of enzyme mL−1. The rationale underlying the effect on the catalytic parameters due to the F238A substitution was studied by enzymatic investigation and molecular dynamics/docking analysis. The present workflow is a well-suited protocol for the evolution of PHEs to help generate an efficient enzymatic toolbox for polyester degradation.

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Khairul Salleh, Badrul Nazahan, Nardiah Rizwana Jaafar, and Rosli Md Illias. "Molecular and Interactions Modelling of PETase and Its Variant with Different Types of Crosslinker in Enzyme Immobilization." Journal of Bioprocessing and Biomass Technology 1, no. 1 (2022): 13–18. http://dx.doi.org/10.11113/bioprocessing.v1n1.7.

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    Plastics are made from non-renewable resources and due to the tremendous production of plastics nowadays, they can lead to high levels of pollution. Biodegradation of plastic by utilizing enzymatic catalytic reaction is an environmentally friendly strategy that produce less or no negative carbon footprint. PETase from Ideonella sakaiensis (IsPETase) is an enzyme that able to degrade polyethylene terephthalate (PET), a building block of plastic. However, free enzyme has several limitations such as unstable in harsh conditions and lack of reusability. One of the strategies to overcome this drawback is through enzyme immobilization that able to improve the enzymatic properties. A suitable crosslinker is very important as it would determine the interactions of the enzymatic particles. Crosslinker should be chosen before performing the enzyme immobilization and this can be accomplished by molecular docking. Thus, the purpose of this research is to determine the suitability of glutaraldehyde, chitosan, dialdehyde starch (DAS) and ethylene glycol as the crosslinker for IsPETase and its variant. Three-dimensional structure of the enzymes was built and docked with different types of crosslinkers. Binding affinity and interactions between the enzymes and the crosslinkers were analyzed and it was found that chitosan has the lowest binding affinity (-7.9 kcal/mol) and the highest number of interactions. This is followed by DAS, ethylene glycol and glutaraldehyde. By using computational analysis, suitable crosslinker for IsPETase could be determine and this would a cost-effective practice in enzyme immobilization strategy.    

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Tian, Ziming. "Simulation Assisted Improvement of Plastic Degradation Enzyme PETase based Machine Learning Tools." Theoretical and Natural Science 67, no. 1 (2024): 182–95. https://doi.org/10.54254/2753-8818/2024.18882.

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Polyethylene terephthalate (PET) plastic is one of the most widely used plastic primarily due to its flexibility, endurance, and low cost. However, the plastics one-time use nature and long degradation time have led to massive waste accumulation, damaging our ecosystem, health, and biodiversity. While previous degradation methods are ineffective due to their high cost and low efficiency, the discovery of two enzymes PETase and MHETase in the bacteria Ideonella sakaiensis to degrade PET and mono(2-hydroxyethyl), a reaction intermediate in PET degradation, respectively, sparked the idea of a sustainable approach to degradation. Ever since, many approaches, including directed evolution, rational protein engineering, and computational redesign strategies, have optimized PETase in terms of its thermostability, catalytic activity, and more. This study proposes the incorporation of newly developed machine learning-based computational tools, including MutCompute, AlphaFold, and DiffDock, into a holistic protein engineering process to predict optimal PETase mutations. Here, in-silico experiments using machine learning tools as well as molecular dynamics simulation and interactions analysis screened for large amounts of PETase mutants in a time and cost-saving manner. Degradation assay coupled with mass analysis and high-performance liquid chromatography techniques then experimentally characterized PETase and its chosen mutants; thus, further screening found the most viable PETase mutant. Using various strategies, the project directly tackles one of the major global issues sustainability by bio-recycling PET. The research also aims to pave the way for introducing a new, imitable process for the more effective and resource-efficient engineering of all proteins.

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Austin, Harry P., Mark D. Allen, Bryon S. Donohoe, et al. "Characterization and engineering of a plastic-degrading aromatic polyesterase." Proceedings of the National Academy of Sciences 115, no. 19 (2018): E4350—E4357. http://dx.doi.org/10.1073/pnas.1718804115.

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Poly(ethylene terephthalate) (PET) is one of the most abundantly produced synthetic polymers and is accumulating in the environment at a staggering rate as discarded packaging and textiles. The properties that make PET so useful also endow it with an alarming resistance to biodegradation, likely lasting centuries in the environment. Our collective reliance on PET and other plastics means that this buildup will continue unless solutions are found. Recently, a newly discovered bacterium, Ideonella sakaiensis 201-F6, was shown to exhibit the rare ability to grow on PET as a major carbon and energy source. Central to its PET biodegradation capability is a secreted PETase (PET-digesting enzyme). Here, we present a 0.92 Å resolution X-ray crystal structure of PETase, which reveals features common to both cutinases and lipases. PETase retains the ancestral α/β-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases. By narrowing the binding cleft via mutation of two active-site residues to conserved amino acids in cutinases, we surprisingly observe improved PET degradation, suggesting that PETase is not fully optimized for crystalline PET degradation, despite presumably evolving in a PET-rich environment. Additionally, we show that PETase degrades another semiaromatic polyester, polyethylene-2,5-furandicarboxylate (PEF), which is an emerging, bioderived PET replacement with improved barrier properties. In contrast, PETase does not degrade aliphatic polyesters, suggesting that it is generally an aromatic polyesterase. These findings suggest that additional protein engineering to increase PETase performance is realistic and highlight the need for further developments of structure/activity relationships for biodegradation of synthetic polyesters.

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Raut, R. R., A. R. Kurhe, and G. D. Suryawanshi. "Use of Bacteria as an Effective Measure for Plastic Bioremediation." International Journal of Research Studies on Environment, Earth, and Allied Sciences (IJRSEAS) 2, no. 2 (2025): 19–21. https://doi.org/10.5281/zenodo.15323006.

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AbstractPlastic pollution has emerged as a critical and growing ecological issue, posing significant threats to both human health and natural ecosystems. The widespread accumulation of plastic waste in terrestrial and marine environments has led to severe consequences, including harm to wildlife, contamination of water sources, and the release of toxic chemicals into the environment. Traditional methods of plastic waste management, such as incineration and landfilling, are often inadequate and can exacerbate environmental problems by contributing to air pollution, soil contamination, and greenhouse gas emissions. In response to these challenges, bioremediation, particularly through the use of bacteria, offers a promising and sustainable solution for plastic degradation. This review investigates the various mechanisms by which bacteria can break down plastics, including the role of specific bacterial species and enzymes that facilitate the biodegradation process. It identifies the most effective bacterial strains, such as Ideonella sakaiensis, known for its ability to degrade polyethylene terephthalate (PET), and explores the enzymatic pathways involved in plastic decomposition. Furthermore, the review examines the potential of bacterial bioremediation in addressing the global plastic waste crisis, highlighting both its benefits and the challenges it faces. These challenges include the slow rate of degradation, the diversity of plastic polymers, and the environmental conditions required for optimal bacterial activity. Recent advancements in genetic engineering and biotechnology are also discussed as key factors enhancing the efficiency and scalability of bacterial plastic degradation. Innovations such as the development of genetically modified bacteria with improved plastic-degrading capabilities hold promise for accelerating the breakdown of plastics and promoting environmental sustainability. 

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Yoshida, Shosuke. "Ideonella sakaiensisによるポリエチレンテレフタレートを原料としたポリヒドロキシアルカン酸の発酵生産". Sen'i Gakkaishi 80, № 4 (2024): P—132—P—135. http://dx.doi.org/10.2115/fiber.80.p-132.

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Jo'rayeva, Marvarida. "PLASTIK CHIQINDILARNI PARCHALAYDIGAN MIKROORGANIZMLAR." JOURNAL OF ANALYTICAL SYNERGY AND SCIENTIFIC HORIZON 1, no. 1 (2025): 34–41. https://doi.org/10.5281/zenodo.14755419.

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Plastik chiqindilar bugungi ekologik muammolarning eng dolzarblaridan biri hisoblanadi. Ularning parchalanish muddati o‘ta uzoq bo‘lgani sababli, atrof-muhitga zarar yetkazadi. Shunday sharoitda plastik materiallarni biologik yo‘l bilan parchalay oladigan mikroorganizmlarni o‘rganish va amaliyotga joriy etish muhim yo‘nalishga aylandi. Ushbu maqola plastik chiqindilarni parchalay oladigan mikroorganizmlar haqida umumiy ma’lumotlar va ularning ahamiyatini tahlil qiladi

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S., Menaka Devi. "Bio-based recycling of polyethylene terephthalate (PET) and its effectiveness." Abstracts of International Conferences & Meetings (AICM) 1, no. 3 (2021): 13. https://doi.org/10.5281/zenodo.5047569.

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Introduction: The accumulation of polyethylene terephthalate (PET) waste in the environment has led to increasing global concerns because of the extremely low degradation properties of this polymer. The evolution of microbes leading to abilities to degrade certain polymers is very promising and gives us the opportunity to identify and utilize these properties to solve the long-time existing problem of plastic waste. At present, mechanical, and chemical degradation processes of plastics for their recycling are commonly adopted. However, both the methods remain unattractive due to lower quality product in case of mechanical degradation and high cost and pollution effects in case of chemical degradation. Biological degradation serves to be eco-friendly and cost-effective alternative. The present article discusses about the prospects of using micro-organisms to degrade plastic waste in the environment and how it is going to be an extremely important area of research in the upcoming future. Methods: Important research works that have been done in order to find a way to biologically degrade PET is discussed. The various methods of PET degradation and the microbes which have been so far identified to be capable of degrading PET are mentioned. The enzyme involved in degradation for each microorganism is being explored to get a better understanding of the degradation mechanism. In addition, current status of bio-upcycling of PET is being discussed which is an alternative way of managing the ever-increasing build of plastic waste. Results &Discussions: Different types of PET hydrolases have been isolated from fungi as well as bacteria and some of them have shown remarkable degradation of crystalline PET with upto 50% weight loss and in about two to three weeks’ time (1). Some of the PET hydrolases have been characterized to be stable at high temperatures of 50 to 70°C which is an advantage for industrial application as efficient degraders of PET (2). Further, with site directed mutagenesis and protein engineering of the enzymes responsible for PET degradation, significant increase in activity was observed in some cases (3, 4). Further, exploration of microbial enzymes with the ability to degrade the petroleum-based plastics is a major area of current research. The degradation products can be recycled into useful polymers that are industrially important. Conclusions: Many of the PET hydrolases isolated so far from fungi as well as bacteria are able to degrade crystalline PET significantly. The discovery of thermostable PET degrading enzymes is of major interest since they can be used for efficient degradation of PET at high temperatures. The hydrolysis products, ethylene glycol and terephthalic acid, can be used by certain microorganisms which can synthesize biopolymers, such as polyhydroxyalkanoate, that has a wide range of applications in packaging and in medical fields. Thus, the biobased recycling of PET shows an alternative efficient means to solve the problem of ever-increasing plastic waste, and the importance of exploring the wide range of microorganisms present in the environment.   Keywords: PET hydrolases, MHET hydrolases, Polymers, Monomers, Depolymerization References 1. Farzi A, Dehnad A, Fotouhi AF. Biodegradation of polyethylene terephthalate waste using Streptomyces species and kinetic modeling of the process. Biocatal. Agric. Biotechnol. 2018; 17:25-31. 2. Tournier V, Topham CM, Gilles A et al. (2020). An engineered PET depolymerase to break down and recycle plastic bottles. Nature. 2020; 580 (7802): 216–219.     3. Son HF, Cho IJ, Joo S et al. Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation. A.C.S. Catal. 2019; 9:3519–3526. 4. Furukawa M, Kawakami N, Tomizawa A,Miyamoto K. Efficient Degradation of Poly(ethylene terephthalate) with Thermobifida fusca Cutinase Exhibiting Improved Catalytic Activity Generated using Mutagenesis and Additive-based Approaches. Sci. Rep. 2019; 9(1): 16038.

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Walter, Andreas, Laura Sopracolle, Mira Mutschlechner, Martin Spruck, and Christoph Griesbeck. "Biodegradation of different PET variants from food containers by Ideonella sakaiensis." Archives of Microbiology 204, no. 12 (2022). http://dx.doi.org/10.1007/s00203-022-03306-w.

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AbstractThe accumulation of macro-, micro- and nano-plastic wastes in the environment is a major global concern, as these materials are resilient to degradation processes. However, microorganisms have evolved their own biological means to metabolize these petroleum-derived polymers, e.g., Ideonella sakaiensis has recently been found to be capable of utilizing polyethylene terephthalate (PET) as its sole carbon source. This study aims to prove its potential capacity to biodegrade two commercial PET materials, obtained from food packaging containers. Plastic pieces of different crystallinity were simultaneously introduced to Ideonella sakaiensis during a seven-week lasting investigation. Loss in weight, appearance of plastics, as well as growth of Ideonella sakaiensis—through quantitative real-time PCR—were determined. Both plastics were found enzymatically attacked in a two-stage degradation process, reaching biodegradation capacities of up to 96%. Interestingly, the transparent, high crystallinity PET was almost fully degraded first, followed by the colored low-crystallinity PET. Results of quantitative real-time PCR-based gene copy numbers were found in line with experimental results, thus underlining its potential of this method to be applied in future studies with Ideonella sakaiensis.

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Jerves, Carola, Rui Pedro Neves, Saulo L. Da Silva, Maria Joao Joao Ramos, and Pedro Alexandrino Fernandes. "Rate-Enhancing PETase Mutations Determined Through DFT/MM Molecular Dynamics Simulations." New Journal of Chemistry, 2023. http://dx.doi.org/10.1039/d3nj04204a.

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The PETase enzyme from the bacterium Ideonella sakaiensis can degrade Polyethylene terephthalate (PET) back into its polymeric constituents at room temperature, making it an ecologically friendly tool for reducing PET...

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Yin, Qingdian, Jiaxing Zhang, Sen Ma, et al. "Efficient polyethylene terephthalate biodegradation by an engineered Ideonella sakaiensis PETase with a fixed substrate binding W156 residue." Green Chemistry, 2023. http://dx.doi.org/10.1039/d3gc03663d.

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Ideonella sakaiensis PETase (IsPETase) is a unique polyethylene terephthalate (PET) hydrolase that displays great potential for mitigating PET waste under moderate temperatures. Although IsPETase exhibits specific higher activity towards PET,...

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Hachisuka, Shin-ichi, Tarou Nishii, and Shosuke Yoshida. "Development of a Targeted Gene Disruption System in the Poly(Ethylene Terephthalate)-Degrading Bacterium Ideonella sakaiensis and Its Applications to PETase and MHETase Genes." Applied and Environmental Microbiology 87, no. 18 (2021). http://dx.doi.org/10.1128/aem.00020-21.

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The poly(ethylene terephthalate) (PET)-degrading bacterium Ideonella sakaiensis possesses two unique enzymes able to serve in PET hydrolysis. PET hydrolase (PETase) hydrolyzes PET into mono(2-hydroxyethyl) terephthalic acid (MHET) and MHET hydrolase (MHETase) hydrolyzes MHET into terephthalic acid (TPA) and ethylene glycol (EG).

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Burgin, Tucker, Benjamin C. Pollard, Brandon C. Knott, et al. "The reaction mechanism of the Ideonella sakaiensis PETase enzyme." Communications Chemistry 7, no. 1 (2024). http://dx.doi.org/10.1038/s42004-024-01154-x.

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AbstractPolyethylene terephthalate (PET), the most abundantly produced polyester plastic, can be depolymerized by the Ideonella sakaiensis PETase enzyme. Based on multiple PETase crystal structures, the reaction has been proposed to proceed via a two-step serine hydrolase mechanism mediated by a serine-histidine-aspartate catalytic triad. To elucidate the multi-step PETase catalytic mechanism, we use transition path sampling and likelihood maximization to identify optimal reaction coordinates for the PETase enzyme. We predict that deacylation is likely rate-limiting, and the reaction coordinates for both steps include elements describing nucleophilic attack, ester bond cleavage, and the “moving-histidine” mechanism. We find that the flexibility of Trp185 promotes the reaction, providing an explanation for decreased activity observed in mutations that restrict Trp185 motion. Overall, this study uses unbiased computational approaches to reveal the detailed reaction mechanism necessary for further engineering of an important class of enzymes for plastics bioconversion.

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Fujiwara, Ryoga, Rikako Sanuki, Hiroharu Ajiro, Toshiaki Fukui, and Shosuke Yoshida. "Direct fermentative conversion of poly(ethylene terephthalate) into poly(hydroxyalkanoate) by Ideonella sakaiensis." Scientific Reports 11, no. 1 (2021). http://dx.doi.org/10.1038/s41598-021-99528-x.

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AbstractPoly(ethylene terephthalate) (PET) is a widely used plastic in bottles and fibers; its waste products pollute the environment owing to its remarkable durability. Recently, Ideonella sakaiensis 201-F6 was isolated as a unique bacterium that can degrade and assimilate PET, thus paving the way for the bioremediation and bioconversion of PET waste. We found that this strain harbors a poly(hydroxyalkanoate) (PHA) synthesis gene cluster, which is highly homologous with that of Cupriavidus necator, an efficient PHA producer. Cells grown on PET accumulated intracellular PHA at high levels. Collectively, our findings in this study demonstrate that I. sakaiensis can mediate the direct conversion of non-biodegradable PET into environment-friendly plastic, providing a new approach for PET recycling.

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Journal articles on the topic 'Ideonella sakaiensis'

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